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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate.1 Publication

Catalytic activityi

(S)-malate = fumarate + H2O.1 Publication

Enzyme regulationi

Inhibited by ATP and S-2,3-dicarboxyaziridine.1 Publication

Kineticsi

  1. KM=50 µM for L-malate (at pH 7.3 and 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Pathwayi: tricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Fumarate hydratase class I, aerobic (fumA), Fumarate hydratase class II (fumC)
    This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei188Proton donor/acceptorBy similarity1
    Active sitei318By similarity1
    Binding sitei319SubstrateBy similarity1
    Sitei331Important for catalytic activity1

    GO - Molecular functioni

    • fumarate hydratase activity Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciEcoCyc:FUMC-MONOMER.
    ECOL316407:JW1603-MONOMER.
    MetaCyc:FUMC-MONOMER.
    BRENDAi4.2.1.2. 2026.
    SABIO-RKP05042.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class II (EC:4.2.1.2)
    Short name:
    Fumarase C
    Alternative name(s):
    Iron-independent fumarase
    Gene namesi
    Name:fumC
    Ordered Locus Names:b1611, JW1603
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10358. fumC.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi126R → A: Reduces enzyme activity 10-fold. 1 Publication1
    Mutagenesisi127K → D: No effect. 1 Publication1
    Mutagenesisi129H → N: No effect on activity, but the carboxyamide group from Asn129 swings into the B site and replaces S-malate by forming a bifurcated hydrogen bond with Asn131 and Asp132. 2 Publications1
    Mutagenesisi188H → N: Reduces activity 200-fold. 1 Publication1
    Mutagenesisi315E → Q: Reduces activity 10-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001612751 – 467Fumarate hydratase class IIAdd BLAST467

    Proteomic databases

    EPDiP05042.
    PaxDbiP05042.
    PRIDEiP05042.

    Expressioni

    Inductioni

    Under conditions of iron limitation and oxidative stress.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.6 Publications

    Protein-protein interaction databases

    BioGridi4263123. 8 interactors.
    DIPiDIP-9719N.
    IntActiP05042. 14 interactors.
    STRINGi511145.b1611.

    Structurei

    Secondary structure

    1467
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Beta strandi12 – 16Combined sources5
    Helixi24 – 32Combined sources9
    Helixi42 – 61Combined sources20
    Helixi67 – 81Combined sources15
    Turni82 – 85Combined sources4
    Helixi86 – 88Combined sources3
    Beta strandi92 – 95Combined sources4
    Helixi100 – 117Combined sources18
    Helixi130 – 134Combined sources5
    Turni135 – 137Combined sources3
    Helixi140 – 158Combined sources19
    Helixi160 – 177Combined sources18
    Turni178 – 180Combined sources3
    Beta strandi182 – 187Combined sources6
    Beta strandi190 – 196Combined sources7
    Helixi197 – 222Combined sources26
    Turni230 – 232Combined sources3
    Helixi242 – 254Combined sources13
    Helixi264 – 269Combined sources6
    Helixi272 – 298Combined sources27
    Beta strandi302 – 305Combined sources4
    Beta strandi308 – 310Combined sources3
    Helixi328 – 352Combined sources25
    Helixi362 – 386Combined sources25
    Helixi388 – 390Combined sources3
    Helixi395 – 404Combined sources10
    Helixi406 – 408Combined sources3
    Helixi409 – 413Combined sources5
    Turni414 – 416Combined sources3
    Helixi418 – 431Combined sources14
    Helixi435 – 441Combined sources7
    Helixi447 – 453Combined sources7
    Helixi456 – 458Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FUOX-ray1.98A/B1-467[»]
    1FUPX-ray2.30A/B1-467[»]
    1FUQX-ray2.00A/B1-467[»]
    1FURX-ray1.95A/B1-467[»]
    1KQ7X-ray2.60A/B1-467[»]
    1YFEX-ray2.19A1-467[»]
    2FUSX-ray2.20A/B1-467[»]
    ProteinModelPortaliP05042.
    SMRiP05042.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05042.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni98 – 100Substrate binding3
    Regioni129 – 132B site4
    Regioni139 – 141Substrate binding3
    Regioni187 – 188Substrate bindingBy similarity2
    Regioni324 – 326Substrate bindingBy similarity3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C9Q. Bacteria.
    COG0114. LUCA.
    HOGENOMiHOG000061736.
    InParanoidiP05042.
    KOiK01679.
    OMAiFAYLKKA.
    PhylomeDBiP05042.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00743. FumaraseC. 1 hit.
    InterProiIPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00979. fumC_II. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05042-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL
    60 70 80 90 100
    TKRAAAKVNE DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT
    110 120 130 140 150
    QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV
    160 170 180 190 200
    AALLALRKQL IPQLKTLTQT LNEKSRAFAD IVKIGRTHLQ DATPLTLGQE
    210 220 230 240 250
    ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL
    260 270 280 290 300
    AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS
    310 320 330 340 350
    GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG
    360 370 380 390 400
    GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ
    410 420 430 440 450
    LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF
    460
    DSWVRPEQMV GSMKAGR
    Length:467
    Mass (Da):50,489
    Last modified:August 13, 1987 - v1
    Checksum:i3D67E3C0F0FDF40B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X04065 Genomic DNA. Translation: CAA27698.1.
    U00096 Genomic DNA. Translation: AAC74683.1.
    AP009048 Genomic DNA. Translation: BAA15349.1.
    X00522 Genomic DNA. Translation: CAA25205.1.
    PIRiS07138. UFEC.
    RefSeqiNP_416128.1. NC_000913.3.
    WP_001099085.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74683; AAC74683; b1611.
    BAA15349; BAA15349; BAA15349.
    GeneIDi946147.
    KEGGiecj:JW1603.
    eco:b1611.
    PATRICi32118524. VBIEscCol129921_1682.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X04065 Genomic DNA. Translation: CAA27698.1.
    U00096 Genomic DNA. Translation: AAC74683.1.
    AP009048 Genomic DNA. Translation: BAA15349.1.
    X00522 Genomic DNA. Translation: CAA25205.1.
    PIRiS07138. UFEC.
    RefSeqiNP_416128.1. NC_000913.3.
    WP_001099085.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FUOX-ray1.98A/B1-467[»]
    1FUPX-ray2.30A/B1-467[»]
    1FUQX-ray2.00A/B1-467[»]
    1FURX-ray1.95A/B1-467[»]
    1KQ7X-ray2.60A/B1-467[»]
    1YFEX-ray2.19A1-467[»]
    2FUSX-ray2.20A/B1-467[»]
    ProteinModelPortaliP05042.
    SMRiP05042.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263123. 8 interactors.
    DIPiDIP-9719N.
    IntActiP05042. 14 interactors.
    STRINGi511145.b1611.

    Proteomic databases

    EPDiP05042.
    PaxDbiP05042.
    PRIDEiP05042.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74683; AAC74683; b1611.
    BAA15349; BAA15349; BAA15349.
    GeneIDi946147.
    KEGGiecj:JW1603.
    eco:b1611.
    PATRICi32118524. VBIEscCol129921_1682.

    Organism-specific databases

    EchoBASEiEB0353.
    EcoGeneiEG10358. fumC.

    Phylogenomic databases

    eggNOGiENOG4105C9Q. Bacteria.
    COG0114. LUCA.
    HOGENOMiHOG000061736.
    InParanoidiP05042.
    KOiK01679.
    OMAiFAYLKKA.
    PhylomeDBiP05042.

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER01007.
    BioCyciEcoCyc:FUMC-MONOMER.
    ECOL316407:JW1603-MONOMER.
    MetaCyc:FUMC-MONOMER.
    BRENDAi4.2.1.2. 2026.
    SABIO-RKP05042.

    Miscellaneous databases

    EvolutionaryTraceiP05042.
    PROiP05042.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00743. FumaraseC. 1 hit.
    InterProiIPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00979. fumC_II. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFUMC_ECOLI
    AccessioniPrimary (citable) accession number: P05042
    Secondary accession number(s): P76891
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: November 2, 2016
    This is version 161 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.